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Structure and ligand recognition of the phosphotyrosine binding domain of Shc

Abstract

The nuclear magnetic resonance structure of the phosphotyrosine binding (PTB) domain of She complexed to a phosphopeptide reveals an alternative means of recognizing tryosine-phosphorylated proteins. Unlike in SH2 domains, the phosphopeptide forms an antiparallel β-strand with a β-sheet of the protein, interacts with a hydrophobic pocket through the (pY–5) residue, and adopts a β-turn. The PTB domain is structurally similar to pleckstrin homology domains (a β-sandwich capped by an α-helix) and binds to acidic phospholipids, suggesting a possible role in membrane localization.

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References

  1. Giorgetti, S., Pelicci, P. G., Pelicci, G. & Van Obberghen, E. Eur. J. Biochem. 223, 195–202 (1994).

    Article  CAS  Google Scholar 

  2. Pelicci, G. et al. Cell 70, 93–104 (1992).

    Article  CAS  Google Scholar 

  3. Rozakis-Adcock, M. et al. Nature 360, 689–692 (1992).

    Article  ADS  CAS  Google Scholar 

  4. Stephens, R. M. et al. Neuron 12, 691–705 (1994).

    Article  CAS  Google Scholar 

  5. Obermeier, A. et al. EMBO J. 13, 1585–1590 (1994).

    Article  CAS  Google Scholar 

  6. Ravichandran, K. S. & Burakoff, S. J. J. biol. Chem. 269, 1599–1602 (1993).

    Google Scholar 

  7. Burns, L. A., Karnitz, L. M., Sutor, S. L. & Abraham, R. T. J. biol. Chem. 268, 17659–17661 (1993).

    CAS  PubMed  Google Scholar 

  8. Sato, N., Sakamaki, K., Terada, N., Arai, K. & Miyajima, A. EMBO J. 12, 4181–4189 (1993).

    Article  CAS  Google Scholar 

  9. Ravichandran, K. S. et al. Science 262, 902–905 (1993).

    Article  ADS  CAS  Google Scholar 

  10. Saxton, T., van Oostveen, I., Bowtell, D., Aebersold, R. & Gold, M. J. Immun. 153, 623–636 (1994).

    CAS  PubMed  Google Scholar 

  11. Egan, S. E. Nature 363, 45–51 (1993).

    Article  ADS  CAS  Google Scholar 

  12. van Biesen, T. et al. Nature 376, 781–784 (1995).

    Article  ADS  CAS  Google Scholar 

  13. Lev, S. et al. Nature 376, 737–745 (1995).

    Article  ADS  CAS  Google Scholar 

  14. Kavanaugh, W. M. & Williams, L. T. Science 266, 1862–1865 (1994).

    Article  ADS  CAS  Google Scholar 

  15. Blaikie, P. et al. J. biol. Chem. 269, 32031–32034 (1994).

    CAS  PubMed  Google Scholar 

  16. Gustafson, T. A., He, W., Craparo, A., Schaub, C. D. & O'Neill, T. J. Molec. cell. Biol. 15, 2500–2508 (1995).

    Article  CAS  Google Scholar 

  17. Songyang, Z. et al. Molec. cell. Biol. 14, 2777–2785 (1994).

    Article  CAS  Google Scholar 

  18. Songyang, Z., Margolis, B., Chaudhur, M., Shoelson, S. E. & Cantley, L. C. J. biol. Chem. 270, 14863–14866 (1995).

    Article  CAS  Google Scholar 

  19. Trüb, T. et al. J. biol. Chem. 270, 18205–18208 (1995).

    Article  Google Scholar 

  20. Kavanaugh, W. M., Turck, C. W. & Williams, L. T. Science 268, 1177–1179 (1995).

    Article  ADS  CAS  Google Scholar 

  21. van der Geer, P. et al. Curr. Biol. 5, 404–412 (1995).

    Article  CAS  Google Scholar 

  22. Zhou, M.-M. et al. J. biol. Chem. 270, 31119–31123 (1995).

    Article  CAS  Google Scholar 

  23. Dikic, I. et al. J. biol. Chem. 270, 15125–15129 (1985).

    Article  Google Scholar 

  24. O'Neill, T. J., Craparo, A. & Gustafson, T. A. Molec. cell. Biol. 14, 6433–6442 (1994).

    Article  CAS  Google Scholar 

  25. Bork, P. & Margolis, B. Cell 80, 693–694 (1995).

    Article  CAS  Google Scholar 

  26. Sun, X. J. et al. Nature 377, 173–177 (1995).

    Article  ADS  CAS  Google Scholar 

  27. Yamazaki, T., Lee, W., Arrowsmith, C. H., Muhandiram, D. R. & Kay, L. E. J. Am. chem. Soc. 116, 11655–11666 (1994).

    Article  CAS  Google Scholar 

  28. Nilges, M., Clore, G. M. & Gronenborn, A. M. FEBS Lett. 229, 317–324 (1988).

    Article  CAS  Google Scholar 

  29. Kuszewski, J., Nilges, M. & Brünger, A. T. J. biomolec. NMR 2, 33–56 (1992).

    Article  CAS  Google Scholar 

  30. Wilmot, C. M. & Tnornton, J. M. J. molec. Biol. 203, 221–232 (1988).

    Article  CAS  Google Scholar 

  31. Bansal, A. & Gierasch, L. M. Cell 67, 1195–1201 (1991).

    Article  CAS  Google Scholar 

  32. Eck, M. J., Shoelson, S. E., & Harrison, S. C. Nature 362, 87–91 (1993).

    Article  ADS  CAS  Google Scholar 

  33. Waksman, G., Shoelson, S. E., Pant, N., Cowburn, D. & Kuriyan, J. Cell 72, 779–790 (1993).

    Article  CAS  Google Scholar 

  34. Zhou, M.-M. et al. Proc. natn. Acad. Sci. U.S.A. 92, 7784–7788 (1995).

    Article  ADS  CAS  Google Scholar 

  35. Flower, D. R. FEBS Lett. 333, 99–102 (1993).

    Article  CAS  Google Scholar 

  36. Saraste, M. & Hyvönen, M. Curr. Opin. struct. Biol. 5, 403–408 (1995).

    Article  CAS  Google Scholar 

  37. Musacchio, A. et al. Trends biochem. Sci. 18, 343–348 (1993).

    Article  CAS  Google Scholar 

  38. Touhara, K. et al. J. biol. Chem. 269, 10217–10220 (1994).

    CAS  Google Scholar 

  39. Harlan, J. E., Hajduk, P. J., Yoon, H. S. & Fesik, S. W. Nature 371, 168–170 (1994).

    Article  ADS  CAS  Google Scholar 

  40. Silvius, J. R. & I'Heureax, F. Biochemistry 33, 3014–3022 (1994).

    Article  CAS  Google Scholar 

  41. Peitzsch, R. M. & Mclaughlin, S. Biochemistry 32, 10436–10443 (1993).

    Article  CAS  Google Scholar 

  42. Brooks, B. R. et al. J. comput. Chem. 4, 187–217 (1983).

    Article  CAS  Google Scholar 

  43. Carson, M. J. molec. Graph. 5, 103–106 (1987).

    Article  CAS  Google Scholar 

  44. Clore, G. M. & Gronenborn, A. M. Meth. Enzym. 239, 349–363 (1994).

    Article  CAS  Google Scholar 

  45. Brünger, A. T. X-PLOR Manual, version 3.1 (Yale Univ. Press, Cambridge, MA, 1992).

    Google Scholar 

  46. Kuboniwa, H., Grzesiek, S., Delaglio, F. & Bax, A. J. biomolec. NMR 4, 871–878 (1994).

    Article  CAS  Google Scholar 

  47. Yoon, H. S. et al. Nature 369, 672–675 (1994).

    Article  ADS  CAS  Google Scholar 

  48. Hope, M. J., Bally, M. B., Webb, G. & Cullis, P. R. Biochim. biophys. Acta 812, 55–65 (1985).

    Article  CAS  Google Scholar 

  49. Tortorella, D. & London, E. Analyt. Biochem. 217, 176–180 (1994).

    Article  CAS  Google Scholar 

  50. Rebecchi, M., Peterson, A. & McLaughlin, S. Biochemistry 31, 12742–12747 (1992).

    Article  CAS  Google Scholar 

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Zhou, MM., Ravichandran, K., Olejniczak, E. et al. Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature 378, 584–592 (1995). https://doi.org/10.1038/378584a0

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